ArticleIntrinsically disordered proteins2015
Can proteins be intrinsically disordered inside a membrane?
Article in Intrinsically disordered proteins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Insights into Membrane Curvature Sensing and Membrane Remodeling by Intrinsically Disordered Proteins and Protein Regions.The Journal of membrane biology · 2022Review
- Assessing the Expression of Aquaporin 3 Antigen-Recognition Sites in Oral Squamous Cell Carcinoma.Applied immunohistochemistry & molecular morphology : AIMM · 2020Article
- Functions of intrinsic disorder in transmembrane proteins.Cellular and molecular life sciences : CMLS · 2017Review
- Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins.The Journal of biological chemistry · 2016Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
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Abstract
Intrinsically disorder has evolved in many soluble proteins because it confers a unique set of functional advantages. In contrast, the functions of membrane proteins are largely understood in terms of well-defined structures. This raises the question: Why would the evolutionary pressures that select for disorder leave membrane proteins untouched. In this hypothesis piece, I argue that intrinsic disorder may exist in membrane embedded proteins, but that it will take a different form due to the different environment. Disordered membrane proteins are thus likely to have fully formed secondary structure, but little tertiary structure. Furthermore, the sequence signature for disorder in membrane proteins is likely to be reversed; so disordered proteins are more hydrophobic than their folded counterparts. At present it is impossible to tell how common this type of disordered membrane protein is.
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Registered trials
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